Q9PTU6 · ENDOU_PAROL
- ProteinUridylate-specific endoribonuclease
- Geneendou
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids385 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
Function
function
Endoribonuclease that cleaves single-stranded RNAs at 5' of uridylates and releases a product with a 2',3'-cyclic phosphate at the 3'-end. The UU and GU sites are more efficiently cleaved than CU and AU sites.
Catalytic activity
- ribonucleotidyl-uridine-RNA = a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + a 5'-end dephospho-uridine-RNAThis reaction proceeds in the forward direction.
Cofactor
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 261 | |||||
Sequence: H | ||||||
Active site | 276 | |||||
Sequence: H | ||||||
Active site | 319 | |||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | lyase activity | |
Molecular Function | metal ion binding | |
Molecular Function | polysaccharide binding | |
Molecular Function | RNA binding | |
Molecular Function | RNA endonuclease activity | |
Molecular Function | scavenger receptor activity | |
Biological Process | immune response |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameUridylate-specific endoribonuclease
- EC number
- Alternative names
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Neoteleostei > Acanthomorphata > Carangaria > Pleuronectiformes > Pleuronectoidei > Paralichthyidae > Paralichthys
Accessions
- Primary accessionQ9PTU6
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-21 | |||||
Sequence: MKVIALLTLCVTLFCQGYSNS | ||||||
Chain | PRO_0000394226 | 22-385 | Uridylate-specific endoribonuclease | |||
Sequence: LDSCQGRCGYGTDNNFSCQCNTSCERFKDCCSDYAEQCKAGATSCKGRCDEKYNSQNKCHCNSKCSRYNNCCSDYTDICDSDAGGGGSVITDADIKAVSEVLYALDSNKATASELIIDPQALVHDSQTSSQRDLSSRPLFRYVDGTLLSRPTYAAFLAVLDNYHRMTGQVEDFSPQQLSEQETFIKEAMSNTELGRELFAFLYTKGVYASENEFLHDLKMMWFGLYSRYNNKMDSSGFEHIFAGEIKGGKVSGFHNWIQFYRLEKRGQLNYYSHSFNGPWTTFPDVMGMQFKWDGYFKQVGSAVIGCSPEFDFALYSLCYITRPGKQCRLSLGGKELIIQTYTWDKTTYGNGKKFIASAFPSTP | ||||||
Disulfide bond | 25↔29 | Alternate | ||||
Sequence: CQGRC | ||||||
Disulfide bond | 25↔41 | Alternate | ||||
Sequence: CQGRCGYGTDNNFSCQC | ||||||
Disulfide bond | 29↔59 | Alternate | ||||
Sequence: CGYGTDNNFSCQCNTSCERFKDCCSDYAEQC | ||||||
Disulfide bond | 39↔41 | Alternate | ||||
Sequence: CQC | ||||||
Disulfide bond | 39↔52 | Alternate | ||||
Sequence: CQCNTSCERFKDCC | ||||||
Disulfide bond | 45↔51 | |||||
Sequence: CERFKDC | ||||||
Disulfide bond | 52↔59 | Alternate | ||||
Sequence: CSDYAEQC | ||||||
Disulfide bond | 66↔70 | Alternate | ||||
Sequence: CKGRC | ||||||
Disulfide bond | 66↔82 | Alternate | ||||
Sequence: CKGRCDEKYNSQNKCHC | ||||||
Disulfide bond | 70↔100 | Alternate | ||||
Sequence: CDEKYNSQNKCHCNSKCSRYNNCCSDYTDIC | ||||||
Disulfide bond | 80↔82 | Alternate | ||||
Sequence: CHC | ||||||
Disulfide bond | 80↔93 | Alternate | ||||
Sequence: CHCNSKCSRYNNCC | ||||||
Disulfide bond | 86↔92 | |||||
Sequence: CSRYNNC | ||||||
Disulfide bond | 93↔100 | Alternate | ||||
Sequence: CSDYTDIC |
Keywords
- PTM
Expression
Tissue specificity
Specifically expressed by the exocrine pancreatic acinar cells.
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 22-61 | SMB 1 | ||||
Sequence: LDSCQGRCGYGTDNNFSCQCNTSCERFKDCCSDYAEQCKA | ||||||
Domain | 62-105 | SMB 2 | ||||
Sequence: GATSCKGRCDEKYNSQNKCHCNSKCSRYNNCCSDYTDICDSDAG | ||||||
Domain | 112-385 | EndoU | ||||
Sequence: TDADIKAVSEVLYALDSNKATASELIIDPQALVHDSQTSSQRDLSSRPLFRYVDGTLLSRPTYAAFLAVLDNYHRMTGQVEDFSPQQLSEQETFIKEAMSNTELGRELFAFLYTKGVYASENEFLHDLKMMWFGLYSRYNNKMDSSGFEHIFAGEIKGGKVSGFHNWIQFYRLEKRGQLNYYSHSFNGPWTTFPDVMGMQFKWDGYFKQVGSAVIGCSPEFDFALYSLCYITRPGKQCRLSLGGKELIIQTYTWDKTTYGNGKKFIASAFPSTP |
Sequence similarities
Belongs to the ENDOU family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length385
- Mass (Da)43,256
- Last updated2000-05-01 v1
- ChecksumA1AE0AA4C461C4C9
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB035673 EMBL· GenBank· DDBJ | BAA88246.1 EMBL· GenBank· DDBJ | mRNA |